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203 118 118 2 2 Peter H. Seidl Karl H. Schleifer Lehrstuhl für Mikrobiologie der Technischen Universität München Arcisstr. 21 D-8000 München 2 Federal Republic of Germany Abstract The synthetic peptides Gly 5 -ε-Ahx and l -Ala 3 -ε-Ahx, with structural similarity to the interpeptide bridge peptides of staphylococci or micrococci, respectively, were covalently linked to human serum albumin via their carboxylgroups. Antisera to these synthetic peptidyl-protein antigens contained fairly high amounts of antibodies with specificity to the N-terminal parts of the peptide chains attached to the carrier proteins. Antisera to (Gly 5 -ε-Ahx) 20 -albumin gave, without exception, strong precipitin reactions in latex-agglutination with staphylococcal peptidoglycans. The antisera completely failed, however, in any reaction with peptidoglycans of micrococci or other bacteria which did not have these oligo-glycine peptides typical for staphylococci. On the contrary, antisera to ( l -Ala 3 -ε-Ahx) 22 -albumin strongly precipitated micrococcal peptidoglycans with oligo- l -alanine interpeptide bridges (e.g. Micrococcus varians, Micrococcus reseus ), but showed no significant reaction with peptidoglycans of staphylococci or other bacteria lacking oligo- l -alanine interpeptide bridges.
Archives of Microbiology – Springer Journals
Published: Aug 1, 1978
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